Spatially Explicit Assessment of Sandhill Crane Exposure to Potential Transmission Line Collision Risk

Infrastructure development can affect avian populations through direct collision mortality. Estimating the exposure of local bird populations to the risk of direct mortality from infrastructure development requires site- and species-specific data, which managers may find difficult to obtain at the scale over which management decisions are made. We quantify the potential exposure of sandhill cranes (Antigone canadensis) to collision with horizontal structures (e.g., transmission lines) within vital wintering grounds of the Middle Rio Grande Valley (MRGV), New Mexico, USA, 2014–2020. Limited maneuverability and visual acuity make sandhill cranes vulnerable to collisions with infrastructure bisecting their flight paths. We used data from 81 global positioning system (GPS)-tagged cranes to estimate the spatially explicit flight height distribution along the MRGV, the passage rate across hypothetical transmission lines, and the resulting exposure rate (exposed passes/crane/day). The exposure rate ranged from 0–0.28 exposed passes/crane/day (median = 0.015) assuming an exposure zone of 7–60 m above ground level, and identified hotspots of potential exposure within the MRGV. Mapped exposure rates can assist in the siting of proposed high-voltage transmission lines, or other infrastructure, to limit effects on sandhill cranes and other avian species at risk of collision. Our approach can be replicated and applied in similar situations where birds are exposed to possible collision with power lines. © 2021 The Authors. The Journal of Wildlife Management published by Wiley Periodicals LLC on behalf of The Wildlife Society.     

Evaluation of a D-amino-acid-containing fluorescence resonance energy transfer peptide library for profiling prokaryotic proteases

Bacterial proteases play an important role in a broad spectrum of processes, including colonization, proliferation, and virulence. In this respect, bacterial proteases are potential biomarkers for bacterial diagnosis and targets for novel therapeutic protease inhibitors. To investigate these potential functions, the authors designed and used a protease substrate fluorescence resonance energy transfer (FRET) library comprising 115 short d- and l-amino-acid-containing fluorogenic substrates as a tool to generate proteolytic profiles for a wide range of bacteria. Bacterial specificity of the d-amino acid substrates was confirmed using enzymes isolated from both eukaryotic and prokaryotic organisms. Interestingly, bacterial proteases that are known to be involved in housekeeping and nutrition, but not in virulence, were able to degrade substrates in which a d-amino acid was present. Using our FRET peptide library and culture supernatants from a total of 60 different bacterial species revealed novel, bacteria-specific, proteolytic profiles, although in-species variation was observed for Pseudomonas aeruginosa, Porphyromonas gingivalis, and Staphylococcus aureus. Overall, the specific characteristic of our substrate peptide library makes it a rapid tool to high-throughput screen for novel substrates to detect bacterial proteolytic activity.     

ATP and the core "alpha-Crystallin" domain of the small heat-shock protein alphaB-crystallin

Electrospray ionization mass spectrometry (ESI-LC/MS) of tryptic digests of human alphaB-crystallin in the presence and absence of ATP identified four residues located within the core "alpha-crystallin" domain, Lys(82), Lys(103), Arg(116), and Arg(123), that were shielded from the action of trypsin in the presence of ATP. In control experiments, chymotrypsin was used in place of trypsin. The chymotryptic fragments of human alphaB-crystallin produced in the presence and absence of ATP were analyzed using liquid chromatography-tandem mass spectrometry (LC-MS/MS). Seven chymotryptic cleavage sites, Trp(60), Phe(61), Phe(75), Phe(84), Phe(113), Phe(118), and Tyr(122), located near or within the core alpha-crystallin domain, were shielded from the action of chymotrypsin in the presence of ATP. Chemically similar analogs of ATP were less protective than ATP against proteolysis by trypsin or chymotrypsin. ATP had no effect on the enzymatic activity of trypsin and the K(m) for trypsin was 0.031 mM in the presence of ATP and 0.029 mM in the absence of ATP. The results demonstrated an ATP-dependent structural modification in the core alpha-crystallin domain conserved in nearly all identified small heat-shock proteins that act as molecular chaperones.